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Conserved domains on  [gi|1002232354|ref|XP_015616421|]
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homeobox-DDT domain protein RLT2 isoform X2 [Oryza sativa Japonica Group]

Protein Classification

DDT and WSD domain-containing protein( domain architecture ID 12039737)

protein containing domains DDT, HARE-HTH, WHIM1, and WSD

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 919-993 3.71e-23

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


:

Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 94.14  E-value: 3.71e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232354  919 YRSLPLGQDRRRNRYWQFstsaspnDPGSGRIFFE-CRDGYWRVLDTEEAFDSLVASLDTRGSREAQLHSMLQRIE 993
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVEsPSDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 344-399 1.23e-17

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


:

Pssm-ID: 460696  Cd Length: 58  Bit Score: 78.32  E-value: 1.23e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232354  344 DNVGNLLMVWKFSITFADVLGLSSVTFDEFVQSLHDYD--SRLLGELHIALLKSIIKD 399
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEepSELLDEIHCALLKALVRD 58
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 519-587 6.19e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


:

Pssm-ID: 461541  Cd Length: 71  Bit Score: 70.80  E-value: 6.19e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232354  519 GTVKFAAFHVLSLEGsKGLTILEVAERIQKSGLRDlTTSKTPEASIAAALSRDTK---LFERTAPSTYCVKS 587
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRS 70
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 739-784 5.74e-07

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


:

Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 47.49  E-value: 5.74e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1002232354  739 SNQGESWVHGLAEGDYCDLSVEERLNALVALVSVANEGNFIRAVLE 784
Cdd:pfam15612    1 REDLPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
DUF4670 super family cl37896
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 85-297 3.25e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


The actual alignment was detected with superfamily member pfam15709:

Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 51.49  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354   85 SGSGHLPQ-SGRREVLPAVPTDYEMIQSNSDLNSVPvegqygiSQVAGIENSLLPSERRAYHDEDGSRVDRKRKHNEEAK 163
Cdd:pfam15709  264 SERGAFSSdSVVEDPWLSSKYDAEESQVSIDGRSSP-------TQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRD 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  164 IAKEVEAHERRI-----RKELEKQDMMKRK---REEQMRKEMERHDRERRKEEERLLRERqrEQerflREQRREHERMEK 235
Cdd:pfam15709  337 RLRAERAEMRRLeverkRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRLRKQRL--EE----ERQRQEEEERKQ 410

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232354  236 FMQKQSRRAEKQRQKEELRK---EKEAARQKAANERATA--RRIAREYMELVEdECLELMELAAQSK 297
Cdd:pfam15709  411 RLQLQAAQERARQQQEEFRRklqELQRKKQQEEAERAEAekQRQKELEMQLAE-EQKRLMEMAEEER 476
 
Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 919-993 3.71e-23

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 94.14  E-value: 3.71e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232354  919 YRSLPLGQDRRRNRYWQFstsaspnDPGSGRIFFE-CRDGYWRVLDTEEAFDSLVASLDTRGSREAQLHSMLQRIE 993
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVEsPSDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 344-399 1.23e-17

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


Pssm-ID: 460696  Cd Length: 58  Bit Score: 78.32  E-value: 1.23e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232354  344 DNVGNLLMVWKFSITFADVLGLSSVTFDEFVQSLHDYD--SRLLGELHIALLKSIIKD 399
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEepSELLDEIHCALLKALVRD 58
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 519-587 6.19e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


Pssm-ID: 461541  Cd Length: 71  Bit Score: 70.80  E-value: 6.19e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232354  519 GTVKFAAFHVLSLEGsKGLTILEVAERIQKSGLRDlTTSKTPEASIAAALSRDTK---LFERTAPSTYCVKS 587
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRS 70
DDT smart00571
domain in different transcription and chromosome remodeling factors;
343-402 2.72e-13

domain in different transcription and chromosome remodeling factors;


Pssm-ID: 214726  Cd Length: 63  Bit Score: 66.12  E-value: 2.72e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232354   343 EDNVGNLLMVWKFSITFADVLGLS--SVTFDEFVQSLHDYDSR-LLGELHIALLKSIIKDIED 402
Cdd:smart00571    1 NEAFGDLLMVYEFLRSFGKVLGLSpfRATLEDFIAALKCRDQNgLLTEVHVVLLRAILKDEGE 63
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 739-784 5.74e-07

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 47.49  E-value: 5.74e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1002232354  739 SNQGESWVHGLAEGDYCDLSVEERLNALVALVSVANEGNFIRAVLE 784
Cdd:pfam15612    1 REDLPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 85-297 3.25e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 51.49  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354   85 SGSGHLPQ-SGRREVLPAVPTDYEMIQSNSDLNSVPvegqygiSQVAGIENSLLPSERRAYHDEDGSRVDRKRKHNEEAK 163
Cdd:pfam15709  264 SERGAFSSdSVVEDPWLSSKYDAEESQVSIDGRSSP-------TQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRD 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  164 IAKEVEAHERRI-----RKELEKQDMMKRK---REEQMRKEMERHDRERRKEEERLLRERqrEQerflREQRREHERMEK 235
Cdd:pfam15709  337 RLRAERAEMRRLeverkRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRLRKQRL--EE----ERQRQEEEERKQ 410

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232354  236 FMQKQSRRAEKQRQKEELRK---EKEAARQKAANERATA--RRIAREYMELVEdECLELMELAAQSK 297
Cdd:pfam15709  411 RLQLQAAQERARQQQEEFRRklqELQRKKQQEEAERAEAekQRQKELEMQLAE-EQKRLMEMAEEER 476
PTZ00121 PTZ00121
MAEBL; Provisional
 147-285 3.54e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 3.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  147 EDGSRVDRKRKhNEEAKIAKEVEAHERRiRKELEKQDMMKRKRE-----EQMRKEMERHDRERRKEEERLLRERQREQER 221
Cdd:PTZ00121  1543 EEKKKADELKK-AEELKKAEEKKKAEEA-KKAEEDKNMALRKAEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232354  222 FLREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVEDE 285
Cdd:PTZ00121  1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
 
Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 919-993 3.71e-23

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 94.14  E-value: 3.71e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232354  919 YRSLPLGQDRRRNRYWQFstsaspnDPGSGRIFFE-CRDGYWRVLDTEEAFDSLVASLDTRGSREAQLHSMLQRIE 993
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVEsPSDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 344-399 1.23e-17

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


Pssm-ID: 460696  Cd Length: 58  Bit Score: 78.32  E-value: 1.23e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232354  344 DNVGNLLMVWKFSITFADVLGLSSVTFDEFVQSLHDYD--SRLLGELHIALLKSIIKD 399
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEepSELLDEIHCALLKALVRD 58
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 519-587 6.19e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


Pssm-ID: 461541  Cd Length: 71  Bit Score: 70.80  E-value: 6.19e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232354  519 GTVKFAAFHVLSLEGsKGLTILEVAERIQKSGLRDlTTSKTPEASIAAALSRDTK---LFERTAPSTYCVKS 587
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRS 70
DDT smart00571
domain in different transcription and chromosome remodeling factors;
343-402 2.72e-13

domain in different transcription and chromosome remodeling factors;


Pssm-ID: 214726  Cd Length: 63  Bit Score: 66.12  E-value: 2.72e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232354   343 EDNVGNLLMVWKFSITFADVLGLS--SVTFDEFVQSLHDYDSR-LLGELHIALLKSIIKDIED 402
Cdd:smart00571    1 NEAFGDLLMVYEFLRSFGKVLGLSpfRATLEDFIAALKCRDQNgLLTEVHVVLLRAILKDEGE 63
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 739-784 5.74e-07

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 47.49  E-value: 5.74e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1002232354  739 SNQGESWVHGLAEGDYCDLSVEERLNALVALVSVANEGNFIRAVLE 784
Cdd:pfam15612    1 REDLPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 85-297 3.25e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 51.49  E-value: 3.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354   85 SGSGHLPQ-SGRREVLPAVPTDYEMIQSNSDLNSVPvegqygiSQVAGIENSLLPSERRAYHDEDGSRVDRKRKHNEEAK 163
Cdd:pfam15709  264 SERGAFSSdSVVEDPWLSSKYDAEESQVSIDGRSSP-------TQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRD 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  164 IAKEVEAHERRI-----RKELEKQDMMKRK---REEQMRKEMERHDRERRKEEERLLRERqrEQerflREQRREHERMEK 235
Cdd:pfam15709  337 RLRAERAEMRRLeverkRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRLRKQRL--EE----ERQRQEEEERKQ 410

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232354  236 FMQKQSRRAEKQRQKEELRK---EKEAARQKAANERATA--RRIAREYMELVEdECLELMELAAQSK 297
Cdd:pfam15709  411 RLQLQAAQERARQQQEEFRRklqELQRKKQQEEAERAEAekQRQKELEMQLAE-EQKRLMEMAEEER 476
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 151-291 3.33e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.07  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  151 RVDRKRKHNEEAKIAKEVEAHERRIRKElEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQRREH 230
Cdd:pfam13868  195 KAQDEKAERDELRAKLYQEEQERKERQK-EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAED 273

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232354  231 ERMEKfMQKQSRRAEKQRQKEEL-------RKEKEAARQKAANERATARRIAREYMELVEDECLELME 291
Cdd:pfam13868  274 EEIEQ-EEAEKRRMKRLEHRRELekqieerEEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
PTZ00121 PTZ00121
MAEBL; Provisional
 147-285 3.54e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 3.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  147 EDGSRVDRKRKhNEEAKIAKEVEAHERRiRKELEKQDMMKRKRE-----EQMRKEMERHDRERRKEEERLLRERQREQER 221
Cdd:PTZ00121  1543 EEKKKADELKK-AEELKKAEEKKKAEEA-KKAEEDKNMALRKAEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232354  222 FLREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVEDE 285
Cdd:PTZ00121  1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
PTZ00121 PTZ00121
MAEBL; Provisional
 147-284 8.29e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 8.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  147 EDGSRVDRKRKHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQ 226
Cdd:PTZ00121  1197 EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE 1276

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232354  227 RREHERMekfmqkqsRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVED 284
Cdd:PTZ00121  1277 ARKADEL--------KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
PTZ00121 PTZ00121
MAEBL; Provisional
 146-285 1.49e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  146 DEDGSRVDRKRKHNEEAKIAKEVEA----HERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQEr 221
Cdd:PTZ00121  1643 AEEKKKAEELKKAEEENKIKAAEEAkkaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL- 1721

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232354  222 flreQRREHERMEKFMQKQSRRAEKQRQKEELRK---EKEAARQKAANERATARRIAREYMELVEDE 285
Cdd:PTZ00121  1722 ----KKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
PTZ00121 PTZ00121
MAEBL; Provisional
 132-285 1.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  132 IENSLLPSERRAYHDEDGSRVDRKRKHNEEAKIAKEV--EAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEE 209
Cdd:PTZ00121  1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  210 RLLRERQREQERFLREQ---------RREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYME 280
Cdd:PTZ00121  1669 KAEEDKKKAEEAKKAEEdekkaaealKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748


                   ....*
gi 1002232354  281 LVEDE 285
Cdd:PTZ00121  1749 AKKDE 1753
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 153-270 1.65e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  153 DRKRKHNE---EAKIAKEVEAHERRI-RKELE--KQDMMKRKREEQM-RKEMERHDRERRKEEERLLRERQREQERFLRE 225
Cdd:pfam17380  471 ERKRKKLElekEKRDRKRAEEQRRKIlEKELEerKQAMIEEERKRKLlEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1002232354  226 QRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERAT 270
Cdd:pfam17380  551 RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATT 595
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 154-295 9.17e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 9.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  154 RKRKHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEmerhdrerrkeeerllrerqreqerfLREQRREHERm 233
Cdd:pfam13868   35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQE--------------------------LEEQIEEREQ- 87

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232354  234 EKFMQKQSRRAEKQRQKEELRKEKEAARQKAAnERATARRIAREYMELVEDECLELMELAAQ 295
Cdd:pfam13868   88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAE-EKLEKQRQLREEIDEFNEEQAEWKELEKE 148
PTZ00121 PTZ00121
MAEBL; Provisional
 147-299 1.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  147 EDGSRVDRKRKHNEEAKIAKEVE--AHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERflr 224
Cdd:PTZ00121  1454 EEAKKAEEAKKKAEEAKKADEAKkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--- 1530

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232354  225 EQRREHERMEKFMQKqsRRAEKQRQKEELRKEKEAAR----QKAANERATARRIAREYMELVEDECLELMELAAQSKGL 299
Cdd:PTZ00121  1531 EEAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKaeeaKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
PTZ00121 PTZ00121
MAEBL; Provisional
 140-280 1.61e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  140 ERRAYHDEDGSRVDRKRKHNEEAKIAKEV--EAHERRIRKELE--KQDMMKRKREEQMRKEMERHDRERRKEEERllrer 215
Cdd:PTZ00121  1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEakKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232354  216 qreqerflrEQRREHERMEKFMQKQSRRAEKQRQKEELRKEK-EAARQKAANERATARRIAREYME 280
Cdd:PTZ00121  1699 ---------EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKaEEAKKEAEEDKKKAEEAKKDEEE 1755
PTZ00121 PTZ00121
MAEBL; Provisional
 140-277 1.70e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  140 ERRAYHDEDGSRVDRKRKHNEEAKIAKEVE--AHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQR 217
Cdd:PTZ00121  1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  218 EQERflREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIARE 277
Cdd:PTZ00121  1475 AKKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
PTZ00121 PTZ00121
MAEBL; Provisional
 147-285 2.55e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  147 EDGSRVDRKRKHNEE-------AKIAKEVEahERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQ 219
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDknmalrkAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232354  220 ERFLREQRREHERMEKFMQKQSRRAEKQRQK--------EELRKEKEAARQK--AANERATARRIAREYMELVEDE 285
Cdd:PTZ00121  1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKaeedkkkaEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEE 1714
PTZ00121 PTZ00121
MAEBL; Provisional
 133-277 3.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  133 ENSLLPSERRAYHDEDGSRVDRKRKHNEEAKIAKEV---EAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEE 209
Cdd:PTZ00121  1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232354  210 RLLRERQREqerflREQRREHERMEKFmqkQSRRAEKQRQKEELRKEKEAARQKAANERATARRIARE 277
Cdd:PTZ00121  1738 EAEEDKKKA-----EEAKKDEEEKKKI---AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 157-280 3.18e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  157 KHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQErfLREQR-REHERMEK 235
Cdd:pfam17380  376 RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR--LEEERaREMERVRL 453

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1002232354  236 FMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYME 280
Cdd:pfam17380  454 EEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 136-301 9.50e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 9.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  136 LLPSERRAYHDEDGSRVDRKRKHNEEAK------IAKEVEAHERRIR-KELEKQDMMKRKRE-EQMRKEMERHDRERRKE 207
Cdd:pfam17380  406 ILEEERQRKIQQQKVEMEQIRAEQEEARqrevrrLEEERAREMERVRlEEQERQQQVERLRQqEEERKRKKLELEKEKRD 485

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  208 EERLLRERQREQERFLREQRR---EHERMEKFMQK-----QSRRAEKQRQK---EELRKEKEAARQKAANE---RATARR 273
Cdd:pfam17380  486 RKRAEEQRRKILEKELEERKQamiEEERKRKLLEKemeerQKAIYEEERRReaeEERRKQQEMEERRRIQEqmrKATEER 565

                          170       180
                   ....*....|....*....|....*...
gi 1002232354  274 IAREYMELVEDECLELMELAAQSKGLPS 301
Cdd:pfam17380  566 SRLEAMEREREMMRQIVESEKARAEYEA 593
PLN02316 PLN02316
synthase/transferase
 223-279 1.09e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 43.71  E-value: 1.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232354  223 LREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYM 279
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLL 307
PTZ00121 PTZ00121
MAEBL; Provisional
 147-277 1.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  147 EDGSRVDRKRKhNEEAKIAKEV-EAHERRIRKELEKQDMMkRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLRE 225
Cdd:PTZ00121  1519 EEAKKADEAKK-AEEAKKADEAkKAEEKKKADELKKAEEL-KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232354  226 QRREHERMEKFMQKQSRRAEKQRQK-------EELRKEKEAARQKAANERATARRIARE 277
Cdd:PTZ00121  1597 VMKLYEEEKKMKAEEAKKAEEAKIKaeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 134-291 1.90e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  134 NSLLPSERRAYHDEDGSRVDRKRKHNEEAKIAKEV-EAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLL 212
Cdd:pfam02463  652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAEsELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232354  213 RERQREQERFLREQRREHERMEKFmqKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVEDECLELME 291
Cdd:pfam02463  732 DKINEELKLLKQKIDEEEEEEEKS--RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEE 808
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 142-281 2.09e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  142 RAYHDEDGSRVDRKRKHNE-----EAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMerhdrerrkeeerllrerq 216
Cdd:pfam17380  302 RQEKEEKAREVERRRKLEEaekarQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL------------------- 362

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232354  217 reqerflrEQRREHE---RMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMEL 281
Cdd:pfam17380  363 --------ERIRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422
PTZ00121 PTZ00121
MAEBL; Provisional
 147-277 2.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  147 EDGSRVDRKRKHNEEAKIAKEVE--AHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQReqerflr 224
Cdd:PTZ00121  1428 EEKKKADEAKKKAEEAKKADEAKkkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD------- 1500

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002232354  225 EQRREHErmEKFMQKQSRRAEKQRQKEELRKEKEAARQKAAnERATARRIARE 277
Cdd:PTZ00121  1501 EAKKAAE--AKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADE 1550
PTZ00121 PTZ00121
MAEBL; Provisional
 147-284 5.46e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  147 EDGSRVDRKRKHNEEAKIAKEVEAHERRIRKeleKQDMMKRKREEQMRK-EMERHDRERRKEEERLLRERQREQERFLRE 225
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKK---KADAAKKKAEEAKKAaEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232354  226 QRREHERMEKFMQKQ------SRRAEKQRQKEELRKEKEAARQKA--ANERATARRIAREYMELVED 284
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKkkadeaKKKAEEDKKKADELKKAAAAKKKAdeAKKKAEEKKKADEAKKKAEE 1442
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 154-268 7.77e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 38.90  E-value: 7.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  154 RKRKHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEerllrerqreqerflREQRREHERM 233
Cdd:pfam11600    8 QSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEE---------------EKELKEKERR 72

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1002232354  234 EKFMQKQSRRAEKQRQKEELRKEKEAARQKAANER 268
Cdd:pfam11600   73 EKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEK 107
PTZ00121 PTZ00121
MAEBL; Provisional
 133-285 7.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 7.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  133 ENSLLPSERRAYHD----EDGSRVDRKRKHNEEAKIAKEVEAHErRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEE 208
Cdd:PTZ00121  1209 EEERKAEEARKAEDakkaEAVKKAEEAKKDAEEAKKAEEERNNE-EIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232354  209 ERLLRERQREQerflrEQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKaANERATARRIAREYMELVEDE 285
Cdd:PTZ00121  1288 EKKKADEAKKA-----EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADE 1358
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 152-277 8.70e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 8.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  152 VDRKRKHNEEAKIAKEVEAhERRIRKELEKQdMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQRREHE 231
Cdd:pfam13868  215 QERKERQKEREEAEKKARQ-RQELQQAREEQ-IELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1002232354  232 R-MEKFMQ--KQSRRAEKQRQKEELRKEKEAARQKAANERATARRIARE 277
Cdd:pfam13868  293 ReLEKQIEerEEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
PTZ00121 PTZ00121
MAEBL; Provisional
 151-285 9.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 9.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  151 RVDRKRKHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQRREh 230
Cdd:PTZ00121  1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE- 1351

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1002232354  231 ermEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVEDE 285
Cdd:PTZ00121  1352 ---AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 151-284 9.82e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 38.62  E-value: 9.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232354  151 RVDRKRKHNEEAKIAKEvEAHERRIRKELEKQdmmKRKREEQMRKEmerhdrerrkeeeRLLrerqreqerflREQRREH 230
Cdd:pfam15236   47 RERKRQKALEHQNAIKK-QLEEKERQKKLEEE---RRRQEEQEEEE-------------RLR-----------REREEEQ 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1002232354  231 ERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIaREYMELVED 284
Cdd:pfam15236   99 KQFEEERRKQKEKEEAMTRKTQALLQAMQKAQELAQRLKQEQRI-RELAEKGHD 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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